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Protein

Thioredoxin-1

Gene

trxA

Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the thioredoxin-thioredoxin reductase system. Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Stimulates complex formation between sigma factor SigR and its cognate anti-sigma factor RsrA probably by reducing RsrA.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Thioredoxin-1
Short name:
Trx-1
Gene namesi
Name:trxA
Ordered Locus Names:SCO3889
ORF Names:SCH24.11c
OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Taxonomic identifieri100226 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
Proteomesi
  • UP000001973 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110Thioredoxin-1PRO_0000120136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 36Redox-activePROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP52230.

Expressioni

Inductioni

Expressed from 2 promoters, 1 of which (trxBp1) is under control of SigR, and further transiently induced (about 50-fold) by the thiol-oxidizing agent diamide. Part of the trxB-trxA operon.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi100226.SCO3889.

Structurei

Secondary structure

1
110
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Turni10 – 123Combined sources
Helixi13 – 164Combined sources
Turni17 – 193Combined sources
Beta strandi24 – 296Combined sources
Helixi34 – 4916Combined sources
Turni50 – 534Combined sources
Beta strandi55 – 606Combined sources
Turni61 – 633Combined sources
Helixi65 – 706Combined sources
Beta strandi75 – 839Combined sources
Beta strandi86 – 938Combined sources
Helixi97 – 1037Combined sources
Helixi105 – 1084Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T00X-ray1.51A1-110[»]
ProteinModelPortaliP52230.
SMRiP52230. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52230.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 109108ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the thioredoxin family.Curated
Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiP52230.
KOiK03671.
OMAiKKTYTDA.
OrthoDBiEOG6QG8RK.
PhylomeDBiP52230.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P52230-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGTLKHVTD DSFEQDVLKN DKPVLVDFWA AWCGPCRQIA PSLEAIAAEY
60 70 80 90 100
GDKIEIVKLN IDENPGTAAK YGVMSIPTLN VYQGGEVAKT IVGAKPKAAI
110
VRDLEDFIAD
Length:110
Mass (Da):11,892
Last modified:June 1, 2001 - v4
Checksum:i18AA0F89F7E513A8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 962KP → NA in CAA63074 (PubMed:9795152).Curated
Sequence conflicti95 – 962KP → NA in CAA07452 (PubMed:9795152).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92105 Genomic DNA. Translation: CAA63077.1.
X92103 Genomic DNA. Translation: CAA63074.1.
AJ007313 Genomic DNA. Translation: CAA07452.1.
AF031590 Genomic DNA. Translation: AAC03481.1.
AF187159 Genomic DNA. Translation: AAF16002.1.
AL939118 Genomic DNA. Translation: CAB42711.1.
PIRiT36576.
T42061.
RefSeqiNP_628075.1. NC_003888.3.
WP_003975042.1. NC_003888.3.

Genome annotation databases

EnsemblBacteriaiCAB42711; CAB42711; CAB42711.
GeneIDi1099325.
KEGGisco:SCO3889.
PATRICi23737562. VBIStrCoe124346_3962.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92105 Genomic DNA. Translation: CAA63077.1.
X92103 Genomic DNA. Translation: CAA63074.1.
AJ007313 Genomic DNA. Translation: CAA07452.1.
AF031590 Genomic DNA. Translation: AAC03481.1.
AF187159 Genomic DNA. Translation: AAF16002.1.
AL939118 Genomic DNA. Translation: CAB42711.1.
PIRiT36576.
T42061.
RefSeqiNP_628075.1. NC_003888.3.
WP_003975042.1. NC_003888.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T00X-ray1.51A1-110[»]
ProteinModelPortaliP52230.
SMRiP52230. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi100226.SCO3889.

Proteomic databases

PRIDEiP52230.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB42711; CAB42711; CAB42711.
GeneIDi1099325.
KEGGisco:SCO3889.
PATRICi23737562. VBIStrCoe124346_3962.

Phylogenomic databases

eggNOGiENOG4105K63. Bacteria.
COG0526. LUCA.
HOGENOMiHOG000292977.
InParanoidiP52230.
KOiK03671.
OMAiKKTYTDA.
OrthoDBiEOG6QG8RK.
PhylomeDBiP52230.

Miscellaneous databases

EvolutionaryTraceiP52230.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PANTHERiPTHR10438. PTHR10438. 1 hit.
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
PIRSFiPIRSF000077. Thioredoxin. 1 hit.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR01068. thioredoxin. 1 hit.
PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor chromosome and comparison with other eubacteria."
    Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y.
    Gene 217:83-90(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  2. "Partitioning of the linear chromosome during sporulation of Streptomyces coelicolor A3(2) involves an oriC-linked parAB locus."
    Kim H.-J., Calcutt M.J., Schmidt F.J., Chater K.F.
    J. Bacteriol. 182:1313-1320(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: A3(2) / NRRL B-16638.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-471 / A3(2) / M145.
  4. "sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2)."
    Paget M.S., Kang J.G., Roe J.H., Buttner M.J.
    EMBO J. 17:5776-5782(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
    Strain: ATCC BAA-471 / A3(2) / M145.
  5. "RsrA, an anti-sigma factor regulated by redox change."
    Kang J.G., Paget M.S.B., Seok Y.J., Hahn M.Y., Bae J.B., Hahn J.S.
    EMBO J. 18:4292-4298(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION WITH RSRA AS SUBSTRATE.
    Strain: ATCC BAA-471 / A3(2) / M145.
  6. "Expression, purification and X-ray crystallographic analysis of thioredoxin from Streptomyces coelicolor."
    Stefankova P., Maderova J., Barak I., Kollarova M., Otwinowski Z.
    Acta Crystallogr. F 61:164-168(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS).

Entry informationi

Entry nameiTHIO1_STRCO
AccessioniPrimary (citable) accession number: P52230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 1, 2001
Last modified: February 17, 2016
This is version 118 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.